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Updated: Jul 6, 2026
Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
Normal cytochrome C oxidase activity in prion protein gene-deficient mice
Akikazu Sakudo1, Yojiro Taniuchi, Takanori Kobayashi
1Department of Virology, Research Institute for Microbial Diseases, Osaka University, Yamadaoka, Suita, Osaka 565-0871, Japan. sakudo@biken.osaka-u.ac.jp
Abstract:
Cytochrome c oxidases of prion protein (PrP) gene-deficient (Prnp(-/-)) and Prnp(+/+) mice were examined in vivo and in vitro. Non-invasive near-infrared spectra revealed that oxidation of copper and heme a+a(3) in cytochrome c oxidase of Prnp(-/-) mice was similar to that in Prnp(+/+) mice. Biochemical analysis of mitochondrial fractions also supported the results. PrP might not be involved in regulation of cytochrome c oxidase.
